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QUA1_CAEEL
ID   QUA1_CAEEL              Reviewed;        1169 AA.
AC   G5EC21;
DT   08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Protein qua-1 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=qua-1 {ECO:0000312|WormBase:T05C12.10};
GN   ORFNames=T05C12.10 {ECO:0000312|WormBase:T05C12.10};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=16502424; DOI=10.1002/dvdy.20721;
RA   Hao L., Mukherjee K., Liegeois S., Baillie D., Labouesse M., Buerglin T.R.;
RT   "The hedgehog-related gene qua-1 is required for molting in Caenorhabditis
RT   elegans.";
RL   Dev. Dyn. 235:1469-1481(2006).
CC   -!- FUNCTION: Required for cuticle shedding and normal alae morphology and
CC       localization, and subsequently larval development.
CC       {ECO:0000269|PubMed:16502424}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:16502424}. Secreted {ECO:0000269|PubMed:16502424}.
CC       Secreted, extracellular space, extracellular matrix
CC       {ECO:0000305|PubMed:16502424}. Note=Secreted by the underlying
CC       hypodermis. {ECO:0000305|PubMed:16502424}.
CC   -!- TISSUE SPECIFICITY: Transiently expressed in head cells.
CC       {ECO:0000269|PubMed:16502424}.
CC   -!- DEVELOPMENTAL STAGE: Mainly expressed in all hypodermal cells (hyp1 to
CC       hyp11) from the tip of the head to the tip of the tail from late
CC       embryogenesis to adulthood, and expressed in the excretory duct and
CC       pore cells from the 3-fold stage of embryogenesis to adulthood.
CC       Expressed in intestinal and rectal cells, sensilla support cells, and
CC       transiently in the P lineage during the L1 stage of larval development.
CC       Temporal expression during the molt phases from larval development
CC       stage L2 to L4 with high expression prior to and during the L2 and L3
CC       molt, but low expression between the molting phases, and low expression
CC       after the L4 molt. {ECO:0000269|PubMed:16502424}.
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DR   EMBL; BX284602; CAA91313.2; -; Genomic_DNA.
DR   PIR; T23754; T23754.
DR   RefSeq; NP_495725.2; NM_063324.3.
DR   AlphaFoldDB; G5EC21; -.
DR   SMR; G5EC21; -.
DR   STRING; 6239.T05C12.10; -.
DR   MEROPS; C46.A05; -.
DR   EPD; G5EC21; -.
DR   PaxDb; G5EC21; -.
DR   PeptideAtlas; G5EC21; -.
DR   EnsemblMetazoa; T05C12.10.1; T05C12.10.1; WBGene00004264.
DR   GeneID; 174319; -.
DR   KEGG; cel:CELE_T05C12.10; -.
DR   CTD; 174319; -.
DR   WormBase; T05C12.10; CE34989; WBGene00004264; qua-1.
DR   eggNOG; KOG3638; Eukaryota.
DR   HOGENOM; CLU_267484_0_0_1; -.
DR   InParanoid; G5EC21; -.
DR   OMA; SIFAGHN; -.
DR   OrthoDB; 792800at2759; -.
DR   PRO; PR:G5EC21; -.
DR   Proteomes; UP000001940; Chromosome II.
DR   Bgee; WBGene00004264; Expressed in larva and 4 other tissues.
DR   GO; GO:0060102; C:collagen and cuticulin-based cuticle extracellular matrix; IDA:WormBase.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0090597; P:nematode male tail mating organ morphogenesis; IMP:WormBase.
DR   GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR   InterPro; IPR001657; Hedgehog.
DR   InterPro; IPR001767; Hedgehog_Hint.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR006141; Intein_N.
DR   Pfam; PF01079; Hint; 1.
DR   PRINTS; PR00632; SONICHHOG.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Developmental protein; Extracellular matrix;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1169
FT                   /note="Protein qua-1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5003475859"
FT   REGION          261..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          368..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        408..427
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..589
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..775
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        830..868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        880..933
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1169 AA;  116870 MW;  1DAF17FD2EB0BE47 CRC64;
     MRRLSAILPI LLLSNFWPTV ESLNYKCHND QILVVQSFGN DTIRMHCQRL DLCGYQKLKC
     DYDELQPQCG GKLNFVSHVN QKGSTAPVEH TCCNLFNPRS HHSIPTHIGN DCFIYELPDG
     SSNGKKVDPA PADDAPYAVL KNPAEIPEQF DGVTGYRLRL FLLKNKSPPT LLVKGIERRL
     DGYRVTICRP RCTSYDKVVN DNEGAEDGEW KAISWSSWSS SSWSTWARHA FNKAAAEGGE
     AAERIRTRMP IGEKTVAGAA GATGAAGSDK SNINIHVESN GNNNNSFEGG RSSSEKSDGQ
     LNREISGSSE AGAGGKGGAG ADGAAGSGAG AGAGAGTNGN INITVHTDGK SGGNAVAVAN
     ANVTVNGAGG VSTTGTGAQT GNESGLGGSA GTDKAGGKKG GHGDSGDSGN NKNKDNGKGK
     GKGKNDEEDE EDNGDEDGNG KGGNGGNPKG EWDDGDGDED DDGTDGGSKE SGNNGKGKGK
     GSGDGDGNRN GNGDGNGRPK GDGNIKINIH SPDDNDLLEK DENGPNGKGG AGNGNGDGDK
     DNNGKGNGTG DGDGDGNGNG NGLTGDGNGT GDGDNNESGN GNGDGSDKNS GAGAGTKPEN
     REGGDGNGNG TGDGNGDGND NGNGSKGLGT GSGDGKGEGN KSGTPGKSDG KEDGAGSNGS
     GNGKEGDGNK SGGSGKGGAG NGKSGDGSGD GKNNGNGGTG DGKDKNGKGS GSGDNDKSGT
     RAAGKGNAEG NGKGNGNDGK GSGSGDGSGA GGKGDKSDSE SGNEADGKDG KKNEGAGGEA
     AAGSGGANKG GSDGDDDDVD VTDVEVGTKP LTGTKLEELL AKLPNETADG NATGDGNEFG
     TVQTGAKHNA ESSASGIPLV QARSNTVNGG APVPPAPGSG ATGSGTSGSG TSESVTNGSG
     ATESGSTGSG TTGTGTSGTG SSGTGASAAR TSSIAGDAPQ AAVLADTPGA AGAAGGGRSN
     CFSADSLVTT VTGQKRMDEL QIGDYVLVPS SGNVLKYEKV EMFYHREPKT RTNFVVLYTK
     SGRKLSLTGR HLLPVAECSQ VEQYTMNPDG IDVAMRESKY AEKARKGECV LSIDESGEVI
     ADEIVRVGRM TNVGIYSPMT VEGSLIVDGV LSSCFSHLES HSAHKLIFDF IYYVYNAFGL
     LNTNHVDLQP IPTFVSFAQY LSKTVLPFS
 
 
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